PMID:11223528
| Citation |
Breed J, , Kneip S, , Gade J, , Welte W, and Bremer E, (2001) Purification, crystallization and preliminary crystallographic analysis of the periplasmic binding protein ProX from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 57:448-50 |
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| Abstract |
A periplasmic binding protein (ProX) for the compatible solutes glycine betaine and proline betaine from Escherichia coli was crystallized using the hanging-drop vapour-diffusion method. Crystals were grown using a protein concentration of 10 mg ml(-1) and a precipitant of 26-28% PEG 4000 in 50 mM PIPES pH 6.2-6.4. Native diffraction data to 1.93 A resolution have been obtained from crystals at 290 K. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 48.1, b = 55.0, c = 115.7 A, and contain one molecule per asymmetric unit. |
| Links | |
| Keywords |
Betaine/chemistry; Carrier Proteins/chemistry; Carrier Proteins/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Proline/analogs & derivatives; Proline/chemistry; Protein Conformation |
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